P53011: Nucleoporin SEH1 (SEH1)

Nucleoporin SEH1 (SEH1) is a 349-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53011.

Gene
SEH1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
349 residues
Mean pLDDT
87.7
Model
AF-P53011-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.7 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate77%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions11%

What pLDDT means and how to read it

Function

Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. It is also required for normal nuclear morphology. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis

Subunit structure

Component of the nuclear pore complex (NPC). NPC constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. Due to its 8-fold…

Subcellular location

Nucleus, nuclear pore complex, Nucleus membrane, Vacuole membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
3F3FX-ray2.9 ÅA/B/E/F=1-349
8ADLEM2.95 ÅD/E/F/L/M/N=1-349
3F3PX-ray3.2 ÅA/B/E/F/I/J=1-349
9H5KEM3.2 ÅD/E/F/L/M/N=1-349
3EWEX-ray3.5 ÅA/C=1-349
3F3GX-ray3.75 ÅA/B/E/F=1-349
6X08X-ray4.19 ÅA=1-349
4XMMX-ray7.38 ÅC=1-349
8TIEEM8.1 Åe/p=1-349
7N84EM11.6 Åe/p=1-349
7N9FEM37.0 Åe/l=1-349

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